Structure of PDB 3o88 Chain B Binding Site BS01

Receptor Information
>3o88 Chain B (length=358) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ
Ligand information
Ligand IDBSH
InChIInChI=1S/C16H18BNO6S/c19-16(20)14-8-4-7-13(9-14)10-15(17(21)22)18-25(23,24)11-12-5-2-1-3-6-12/h1-9,15,18,21-22H,10-11H2,(H,19,20)/t15-/m0/s1
InChIKeyLCKOZWBVAVBOPR-HNNXBMFYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0B([C@H](Cc1cccc(c1)C(=O)O)NS(=O)(=O)Cc2ccccc2)(O)O
ACDLabs 12.01O=S(=O)(NC(B(O)O)Cc1cccc(C(=O)O)c1)Cc2ccccc2
OpenEye OEToolkits 1.7.0B(C(Cc1cccc(c1)C(=O)O)NS(=O)(=O)Cc2ccccc2)(O)O
CACTVS 3.370OB(O)[CH](Cc1cccc(c1)C(O)=O)N[S](=O)(=O)Cc2ccccc2
CACTVS 3.370OB(O)[C@H](Cc1cccc(c1)C(O)=O)N[S](=O)(=O)Cc2ccccc2
FormulaC16 H18 B N O6 S
Name3-[(2R)-2-[(benzylsulfonyl)amino]-2-(dihydroxyboranyl)ethyl]benzoic acid
ChEMBLCHEMBL1231478
DrugBank
ZINCZINC000195357898
PDB chain3o88 Chain B Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3o88 Design, Synthesis, Crystal Structures, and Antimicrobial Activity of Sulfonamide Boronic Acids as beta-Lactamase Inhibitors
Resolution1.64 Å
Binding residue
(original residue number in PDB)		S64 L119 Q120 Y150 N152 Y221 G317 A318 T319
Binding residue
(residue number reindexed from 1)		S61 L116 Q117 Y147 N149 Y218 G314 A315 T316
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 Y150 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 Y147 G153 E269 K312 A315
Enzyme Commision number 3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3o88, PDBe:3o88, PDBj:3o88
PDBsum3o88
PubMed20945905
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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